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1.14.99.B10
Cu2+
the copper ion alone hardly contributes to affinity, but substrate binding is enhanced for metal-loaded enzymes that are supplied with cyanide
741344
1.14.99.B10
Cu2+
the Cu+ center environment is altered upon substrate binding. The oxidative regioselectivity of LPMO9 enzymes (C1, C4, or both) correlates with distinct structural features of the copper coordination sphere. In strictly C1-oxidizing LPMO9s, access to the solvent-facing axial coordination position is restricted by a conserved tyrosine residue, whereas access to this same position seems unrestricted in C4-oxidizing LPMO9s
736485
1.14.99.B10
Zn2+
Zn2+-shows slightly weaker binding compared with Cu2+
741344
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